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Highly functionalized terpyridines as competitive inhibitors of AKAP-PKA interactions

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Official URL:https://doi.org/10.1002/anie.201304686
PubMed:View item in PubMed
Creators Name:Schaefer, G. and Milic, J and Eldahshan, A and Goetz, F. and Zuehlke, K. and Schillinger, C. and Kreuchwig, A. and Elkins, J.M. and Abdul Azeez, K.R.A. and Oder, A. and Moutty, M.C. and Masada, N. and Beerbaum, M. and Schlegel, B. and Niquet, S. and Schmieder, P. and Krause, G. and von Kries, J.P. and Cooper, D.M.F. and Knapp, S. and Rademann, J. and Rosenthal, W. and Klussmann, E.
Journal Title:Angewandte Chemie International Edition
Journal Abbreviation:Angew Chem Int Ed
Volume:52
Number:46
Page Range:12187-12191
Date:11 November 2013
Keywords:AKAP, Peptide Mimetics, Protein Kinase A, Protein-Protein Interactions, Suzuki Coupling, Terpyridines
Abstract:A good fit: Interactions between A-kinase anchoring proteins (AKAPs) and protein kinase A (PKA) play key roles in a plethora of physiologically relevant processes whose dysregulation causes or is associated with diseases such as heart failure. Terpyridines have been developed as α-helix mimetics for the inhibition of such interactions and are the first biologically active, nonpeptidic compounds that block the AKAP binding site of PKA.
ISSN:1433-7851
Publisher:Wiley (Germany)
Item Type:Article

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